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Protein

Cullin-4

Gene

cul4

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required, indirectly, for activation of ribonucleotide reductase through the degradation of the protein spd1, thereby supplying deoxyribonucleotides for DNA replication and repair. Also has a role as a scaffold for assembling ubiquitin ligases. Component of the rik1-associated E3 ubiquitin ligase complex that shows ubiquitin ligase activity and is required for histone H3K9 methylation. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting swi6/HP1 to methylated histones which leads to transcriptional silencing within centromeric heterochromatin, telomeric regions and at the silent mating-type loci.3 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • cellular protein localization Source: PomBase
  • chromatin silencing at centromere Source: PomBase
  • chromatin silencing at silent mating-type cassette Source: PomBase
  • chromatin silencing at telomere Source: PomBase
  • chromatin silencing by small RNA Source: PomBase
  • heterochromatin assembly Source: PomBase
  • negative regulation of transcription from RNA polymerase II promoter Source: PomBase
  • positive regulation of meiotic cell cycle Source: PomBase
  • protein ubiquitination Source: PomBase
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: PomBase
  • regulation of histone H3-K9 methylation Source: PomBase
  • transcription, DNA-templated Source: UniProtKB-KW
  • transcription-coupled nucleotide-excision repair Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-5696395. Formation of Incision Complex in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-4
Short name:
Cul-4
Gene namesi
Name:cul4
Synonyms:pcu4
ORF Names:SPAC3A11.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC3A11.08.
PomBaseiSPAC3A11.08.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • CLRC ubiquitin ligase complex Source: PomBase
  • cytosol Source: PomBase
  • nuclear pericentric heterochromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi680 – 6801K → R: Increase in H3-K4 methylation within heterochromatin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 734734Cullin-4PRO_0000119810Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki680 – 680Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiO14122.

Interactioni

Subunit structurei

Component of the rik1-associated E3 ubiquitin ligase complex composed of at least clr4, cul4, pip1, raf1 and raf2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
clr4O600163EBI-904890,EBI-354657
rik1Q104263EBI-904890,EBI-1111936

GO - Molecular functioni

Protein-protein interaction databases

BioGridi279548. 11 interactions.
IntActiO14122. 7 interactions.
MINTiMINT-4670656.

Structurei

3D structure databases

ProteinModelPortaliO14122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiO14122.
KOiK10609.
OMAiNIATSER.
OrthoDBiEOG7FJH80.
PhylomeDBiO14122.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14122-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPEAKRIVV KGFDPRKSRQ RQETYYVTMI DRLNMALQVV MAGLGLKTGY
60 70 80 90 100
QELYSGVENL TRADQASRCF NILQHHMSSG IQLLKDSAES FIQLEGTETD
110 120 130 140 150
TNACTVVVGC WNKWLERVEI VQNIFYYMDK TFLSHHPDYP TIEELSLSLF
160 170 180 190 200
REKLMAVKNI QIPFLNSLLQ SFENLHSSKS TDHAYLQDAM LMLHRTEMYS
210 220 230 240 250
SVFVPMYLVM LSRFYDTESS QKIQELPLEE YLEYAMSSLE REDAYVEKFD
260 270 280 290 300
IVRDKKSIRE TVQRCLITSH LDTLTKGISQ FIEKRDAHSC KLLYALLQFN
310 320 330 340 350
HETEYLIQPW SDCLVDVGFK LVNDESKDDT LVQELLSFHK FLQVVVDESF
360 370 380 390 400
LHDETLSYAM RKAFETFING AKGSQREAPA RLIAKYIDYL LRVGEQASGG
410 420 430 440 450
KPLKEVFSEI LDLFRYIASK DIFEAYYKLD IAKRLLLNKS ASAQNELMLL
460 470 480 490 500
DMLKKTCGSQ FTHSLEGMFR DVNISKEFTS SFRHSKAAHN LHRDLYVNVL
510 520 530 540 550
SQAYWPSYPE SHIRLPDDMQ QDLDCFEKFY LSKQVGKKIS WYASLGHCIV
560 570 580 590 600
KARFPLGNKE LSISLFQACV LLQFNNCLGG EGISYQDLKK STELSDIDLT
610 620 630 640 650
RTLQSLSCAR IRPLVMVPKS KKPSPDTMFY VNEKFTDKLY RVKINQIYLK
660 670 680 690 700
EERQENSDVQ EQVVRDRQFE LQASIVRVMK QKEKMKHDDL VQYVINNVKD
710 720 730
RGIPLVSDVK TAIEKLLEKE YLEREDNDIY TYVT
Length:734
Mass (Da):85,330
Last modified:January 1, 1998 - v1
Checksum:iE90FFFE06D071C3E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16383.1.
AB017029 Genomic DNA. Translation: BAA32520.1.
AB027893 Genomic DNA. Translation: BAA87197.1.
PIRiT43408.
RefSeqiNP_594195.1. NM_001019619.2.

Genome annotation databases

EnsemblFungiiSPAC3A11.08.1; SPAC3A11.08.1:pep; SPAC3A11.08.
GeneIDi2543116.
KEGGispo:SPAC3A11.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16383.1.
AB017029 Genomic DNA. Translation: BAA32520.1.
AB027893 Genomic DNA. Translation: BAA87197.1.
PIRiT43408.
RefSeqiNP_594195.1. NM_001019619.2.

3D structure databases

ProteinModelPortaliO14122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279548. 11 interactions.
IntActiO14122. 7 interactions.
MINTiMINT-4670656.

Proteomic databases

MaxQBiO14122.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC3A11.08.1; SPAC3A11.08.1:pep; SPAC3A11.08.
GeneIDi2543116.
KEGGispo:SPAC3A11.08.

Organism-specific databases

EuPathDBiFungiDB:SPAC3A11.08.
PomBaseiSPAC3A11.08.

Phylogenomic databases

InParanoidiO14122.
KOiK10609.
OMAiNIATSER.
OrthoDBiEOG7FJH80.
PhylomeDBiO14122.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-5696395. Formation of Incision Complex in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

PROiO14122.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes together with cullin-1 in fission yeast SCF (Skip-cullin-1-F-box) ubiquitin ligase."
    Kominami K., Ochotorena I., Toda T.
    Genes Cells 3:721-735(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "A Rik1-associated, cullin-dependent E3 ubiquitin ligase is essential for heterochromatin formation."
    Horn P.J., Bastie J.-N., Peterson C.L.
    Genes Dev. 19:1705-1714(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION IN THE RIK1-ASSOCIATED E3 UBIQUITIN LIGASE COMPLEX, MUTAGENESIS OF LYS-680.
  4. "Ubiquitin ligase component Cul4 associates with Clr4 histone methyltransferase to assemble heterochromatin."
    Jia S., Kobayashi R., Grewal S.I.S.
    Nat. Cell Biol. 7:1007-1013(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 180-195; 223-241; 321-340 AND 591-601, FUNCTION, INTERACTION WITH CLR4 AND RIK1.
  5. "Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library."
    Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T., Hiraoka Y.
    Genes Cells 5:169-190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 186-412, SUBCELLULAR LOCATION.
    Strain: ATCC 38364 / 968.
  6. "Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms."
    Liu C., Powell K.A., Mundt K., Wu L., Carr A.M., Caspari T.
    Genes Dev. 17:1130-1140(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "The Clr7 and Clr8 directionality factors and the Pcu4 cullin mediate heterochromatin formation in the fission yeast Schizosaccharomyces pombe."
    Thon G., Hansen K.R., Altes S.P., Sidhu D., Singh G., Verhein-Hansen J., Bonaduce M.J., Klar A.J.
    Genetics 171:1583-1595(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAF2.
  8. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCUL4_SCHPO
AccessioniPrimary (citable) accession number: O14122
Secondary accession number(s): Q9USB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: January 1, 1998
Last modified: July 6, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.